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JCS ePress online publication date 1 Aug 2006
doi: 10.1242/jcs.03067

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Research Article

Activation of urokinase receptor by a novel interaction between the connecting peptide region of urokinase and {alpha}v{beta}5 integrin


Paola Franco, Immacolata Vocca, Maria V. Carriero, Daniela Alfano, Letizia Cito, Immacolata Longanesi-Cattani, Paolo Grieco, Liliana Ossowski, and Maria P. Stoppelli*
* Author for correspondence (e-mail: stoppell{at}igb.cnr.it)

The serine protease urokinase (uPA) binds to the urokinase receptor (uPAR) through its growth-factor domain (GFD, residues 1-49), affecting cell migration, adhesion and growth. Here, we show that uPA can promote cytoskeletal rearrangements and directional cell migration in a GFD-independent manner, through a new and specific interaction between an internal uPA domain coined 'connecting peptide' (residues 132-158) and cell-surface integrin {alpha}v{beta}5. Remarkably, a peptide corresponding to this region (CPp, residues 135-158) retains the ability to bind to {alpha}v{beta}5, eliciting cytoskeletal rearrangements and directing cell migration at a concentration as low as 1-10 pM. These effects are lost in cells not expressing uPAR, indicating that the uPAR is required for CPp-dependent signaling. Furthermore, the CPp-{alpha}v{beta}5-integrin interaction enhances F-actin-enriched protrusions and cell migration induced by the well-established interaction between the uPAR-binding peptide (GFDp, residues 12-32) of uPA and uPAR. These results provide new insight into the function of uPA, which - through individual domains - can engage two different surface receptors (uPAR and {alpha}v{beta}5 integrin), thus initiating and potentiating intracellular signaling and migration.
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